Evidence map›Paper›PMID 28067448›Full record

ArticleChembiochem : a European journal of chemical biology2017

OleD Loki as a Catalyst for Tertiary Amine and Hydroxamate Glycosylation.

Ryan R Hughes, Khaled A Shaaban, Jianjun Zhang, Hongnan Cao, George N Phillips, Jon S Thorson

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Chembiochem : a European journal of chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Article
  2. OleD Loki as a Catalyst for Hydroxamate Glycosylation.Chembiochem : a European journal of chemical biology · 2020
    Article
  3. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Ryan R HughesCenter for Pharmaceutical Research and Innovation, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA.
Khaled A ShaabanCenter for Pharmaceutical Research and Innovation, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA.
Jianjun ZhangCenter for Pharmaceutical Research and Innovation, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA.
Hongnan CaoDepartment of Chemistry, Rice University, P. O. Box 1892, MS 60, Houston, TX, 77251, USA.
George N PhillipsDepartment of Chemistry, Rice University, P. O. Box 1892, MS 60, Houston, TX, 77251, USA.
Jon S ThorsonCenter for Pharmaceutical Research and Innovation, College of Pharmacy, University of Kentucky, 789 South Limestone Street, Lexington, KY, 40536, USA.

Funding

Kentucky Center for Clinical and Translational ScienceUL1TR001998 · NCATS · UNIVERSITY OF KENTUCKY · PI HARTMANN, KATHERINE E, KERN, PHILIP A · 2016 to 2025
$34.2M
Kentucky Center for Clinical and Translational ScienceUL1TR000117 · NCATS · UNIVERSITY OF KENTUCKY · PI KERN, PHILIP A · 2012 to 2015
$13.3M
In Vitro Glycorandomization of Natural ProductsR37AI052218 · NIAID · UNIVERSITY OF KENTUCKY · PI THORSON, JON SCOTT · 2012 to 2021
$4.0M
Enzyme Discovery for Natural Product BiosynthesisU01GM098248 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI PHILLIPS, GEORGE NEAL · 2011 to 2015
$2.8M
NCATS NIH HHS UL1 TR000117NCATS NIH HHS UL1 TR001998NIAID NIH HHS R37 AI052218NIGMS NIH HHS U01 GM098248
6 · The paper itself

Abstract

We describe the ability of an engineered glycosyltransferase (OleD Loki) to catalyze the N-glycosylation of tertiary-amine-containing drugs and trichostatin hydroxamate glycosyl ester formation. As such, this study highlights the first bacterial model catalyst for tertiary-amine N-glycosylation and further expands the substrate scope and synthetic potential of engineered OleDs. In addition, this work could open the door to the discovery of similar capabilities among other permissive bacterial glycosyltransferases.

Indexed as

Models, BiologicalAminesCatalysisCatalytic DomainGlycosylationGlycosyltransferasesHydroxamic AcidsMolecular StructureProtein EngineeringAminesGlycosyltransferasesHydroxamic Acidsantidepressantsdrug metabolismglucuronidationglycosyltransferasestrichostatin

Identifiers

PMID28067448
PMCPMC5355705

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.